A PilZ domain protein for chemotaxis adds another layer to c-di-GMP-mediated regulation of flagellar motility

Mona W Orr; Vincent T Lee

doi:10.1126/scisignal.aai8859

A PilZ domain protein for chemotaxis adds another layer to c-di-GMP-mediated regulation of flagellar motility

Sci Signal. 2016 Oct 18;9(450):fs16. doi: 10.1126/scisignal.aai8859.

Authors

Mona W Orr¹, Vincent T Lee²

Affiliations

¹ Department of Cell Biology and Molecular Genetics and Maryland Pathogen Research Institute, University of Maryland, College Park, College Park, MD 20742, USA.
² Department of Cell Biology and Molecular Genetics and Maryland Pathogen Research Institute, University of Maryland, College Park, College Park, MD 20742, USA. vtlee@umd.edu.

PMID: 27811181
DOI: 10.1126/scisignal.aai8859

Abstract

Cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous second messenger in bacteria. In this issue of Science Signaling, Xu et al show that c-di-GMP regulates chemotaxis by binding to the PilZ domain protein MapZ to alter the methyltransferase activity of its protein partner CheR, fleshing out the c-di-GMP signaling network of the opportunistic pathogen Pseudomonas aeruginosa.

Publication types

Review
Comment

MeSH terms

Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
Chemotaxis / physiology*
Cyclic GMP / analogs & derivatives*
Cyclic GMP / genetics
Cyclic GMP / metabolism
Flagella / genetics
Flagella / metabolism*
Movement / physiology*
Pseudomonas aeruginosa / genetics
Pseudomonas aeruginosa / metabolism*
Second Messenger Systems / physiology*

Substances

Bacterial Proteins
bis(3',5')-cyclic diguanylic acid
Cyclic GMP